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Developments in the characterisation of the catalytic triad of alpha-chymotrypsin: Effect of the protonation state of Asp102 on the 1H NMR signals of His57.

Abstract:
Protonated or not? 1H NMR spectra of α-chymotrypsin were recorded as a function of pH (from top to bottom pH 8.6, 5.1 and 4.2). Slow exchange is observed for the NH protons of His57 between two environments due to different protonation states of Asp102. © 2007 Wiley-VCH Verlag GmbH and Co. KGaA.
Publication status:
Published

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Publisher copy:
10.1002/cbic.200600433

Authors


Bruylants, G More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Chembiochem : a European journal of chemical biology
Volume:
8
Issue:
1
Pages:
51-54
Publication date:
2007-01-05
DOI:
EISSN:
1439-7633
ISSN:
1439-4227
URN:
uuid:fa98e1a4-ec6e-4ded-b295-0c80e736253b
Source identifiers:
100450
Local pid:
pubs:100450

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